Temperature dependence of a diffusion‐limited immobilized enzyme reaction
作者:
K. Buchholz,
W. Rüth,
期刊:
Biotechnology and Bioengineering
(WILEY Available online 1976)
卷期:
Volume 18,
issue 1
页码: 95-104
ISSN:0006-3592
年代: 1976
DOI:10.1002/bit.260180108
出版商: Wiley Subscription Services, Inc., A Wiley Company
数据来源: WILEY
摘要:
AbstractThe apparent activation energy ofN‐α‐benzoyl‐L‐arginine‐ethyl ester (BAEE) hydrolysis by immobilized trypsin varies with the bulk substrate concentration from its maximum value, comparable to that of the free enzyme, to considerably lower values. Thus, with a concentration change from 3 × 10−2to 10−4Mthe apparent activation energy diminishes from 9.5 to 4.5 kcal/mol. This experimental finding is interpreted to be due to Michaelis‐type kinetics in a heterogeneous system, in one case reflecting the temperature dependence of the maximal enzyme reaction rate, in another case illustrating the diffusion limited overall reaction at low substrate concentrations. As a consequence it may not be feasible to operate a reaction at elevated temperatures in a high conversion range, since diffusion limitation may restrict the enhancement of the overall reaction rate. Some further data are given concerning the buffer effect on the reaction rate, which should occur due to its limitation by proton transfer in the b
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